Mechanistic insights into nitrogen fixation by nitrogenase enzymes

被引：85

作者：

Varley, J. B. ^{[1
,2
,3
]}

Wang, Y. ^{[2
]}

Chan, K. ^{[2
]}

Studt, F. ^{[2
,4
]}

Norskov, J. K. ^{[2
,4
]}

机构：

[1] Stanford Univ, Dept Chem Engn, SUNCAT Ctr Interface Sci & Catalysis, Stanford, CA 94305 USA

[2] Stanford Univ, Dept Chem Engn, SUNCAT Ctr Interface Sci & Catalysis, Stanford, CA 94305 USA

[3] Lawrence Livermore Natl Lab, Livermore, CA 94550 USA

[4] SLAC Natl Accelerator Lab, SUNCAT Ctr Interface Sci & Catalysis, Photon Sci, Menlo Pk, CA 94025 USA

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2015年 / 17卷 / 44期

关键词：

DENSITY-FUNCTIONAL THEORY; IRON-MOLYBDENUM COFACTOR; HABER-BOSCH PROCESS; FEMO-COFACTOR; AMMONIA-SYNTHESIS; REDUCTION; CARBON; EVOLUTION; PRESSURE; HYDROGEN;

D O I：

10.1039/c5cp04034e

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Biological nitrogen fixation by nitrogenase enzymes is a process that activates dinitrogen (N-2) one of the most inert molecules in nature, within the confines of a living organism and at ambient conditions. Despite decades of study, there are still no complete explanations as to how this is possible. Here we describe a model of N-2 reduction using the Mo-containing nitrogenase (FeMoco) that can explain the reactivity of the active site via a series of electrochemical steps that reversibly unseal a highly reactive Fe edge site. Our model can explain the 8 proton-electron transfers involved in biological ammonia synthesis within the kinetic scheme of Lowe and Thorneley, the obligatory formation of one H-2 per N-2 reduced, and the behavior of known inhibitors.

引用

页码：29541 / 29547

页数：7

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